What Strengthens Protein-Protein Interactions: Analysis and Applications of Residue Correlation Networks.

ABSTRACT: Identifying residues critical to protein-protein binding and efficient design of stable and specific protein binders are challenging tasks. Extending beyond the direct contacts in a protein-protein binding interface, our study employs computational modeling to reveal the essential network of residue interactions and dihedral angle correlations critical in protein-protein recognition. We hypothesized that mutating residues exhibiting highly correlated dynamic motion within the interaction network could efficiently optimize protein-protein interactions to create tight and selective protein binders. We tested this hypothesis using the ubiquitin (Ub) and MERS coronaviral papain-like protease (PLpro) complex, since Ub is a central player in multiple cellular functions and PLpro is an antiviral

SUBMITTER: Hung TI 

PROVIDER: S-EPMC11637584 | biostudies-literature | 2023 Dec

REPOSITORIES: biostudies-literature